|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-407 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 733.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01663 21 GTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:cd01663 99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFS-NKPV 239
Cdd:cd01663 179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:cd01663 259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:cd01663 339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:cd01663 419 QHFLGLAG 426
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 676.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00153 28 GTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00153 426 QHFLGLAG 433
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-407 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 527.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:TIGR02891 24 GGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLF 320
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 321 TIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPM 400
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPM 420
|
....*..
gi 168418694 401 HFLGLAG 407
Cdd:TIGR02891 421 HLLGLLG 427
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-407 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 518.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:COG0843 33 GGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLF 320
Cdd:COG0843 270 GYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 321 TIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPM 400
Cdd:COG0843 350 VIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPM 429
|
....*..
gi 168418694 401 HFLGLAG 407
Cdd:COG0843 430 HILGLLG 436
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-407 |
1.13e-124 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 367.28 E-value: 1.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:pfam00115 17 GGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMvevGVGTGWTVYPPLssiqshsgASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMyRIPLFVWS 160
Cdd:pfam00115 94 GAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIF-KTPMLFAIGFIFL 319
Cdd:pfam00115 236 GYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:pfam00115 316 FIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFP 395
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:pfam00115 396 MHILGLLG 403
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
1-407 |
0e+00 |
|
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.
Pssm-ID: 238833 Cd Length: 488 Bit Score: 733.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01663 21 GTSLSLLIRLELSQPGS--QLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:cd01663 99 SLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFS-NKPV 239
Cdd:cd01663 179 VLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSgKKPV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:cd01663 259 FGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:cd01663 339 FTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFP 418
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:cd01663 419 QHFLGLAG 426
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 676.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00153 28 GTSLSLLIRAELGQPGS--LIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00153 106 SLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00153 186 VLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKeT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00153 266 FGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00153 346 FTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFP 425
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00153 426 QHFLGLAG 433
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 635.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00167 30 GTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00167 108 SLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00167 188 ILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKeP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00167 268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00167 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00167 428 QHFLGLAG 435
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 622.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00223 27 GTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00223 105 SLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNK-PV 239
Cdd:MTH00223 185 VKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKkEV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00223 265 FGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00223 345 FTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFP 424
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00223 425 QHFLGLAG 432
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 619.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00116 30 GTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00116 108 SFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00116 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKeP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00116 268 FGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00116 348 FTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00116 428 QHFLGLAG 435
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 603.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00142 28 GTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00142 106 ALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWS 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00142 186 VKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKeV 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00142 266 FGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00142 346 FTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFP 425
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00142 426 QHFLGLAG 433
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 578.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00184 32 GTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00184 110 ALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFS-NKPV 239
Cdd:MTH00184 190 ILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAaKKQI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00184 270 FGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00184 350 FTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFP 429
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00184 430 QHFLGLAG 437
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 577.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00182 32 GTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00182 110 ALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNK-PV 239
Cdd:MTH00182 190 ILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKkQI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00182 270 FGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00182 350 FTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFP 429
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00182 430 QHFLGLAG 437
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 549.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00037 30 GTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00037 108 SFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNK-PV 239
Cdd:MTH00037 188 VFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKqEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00037 268 FGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00037 348 FTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00037 428 QHFLGLAG 435
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 544.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00183 30 GTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00183 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFS-NKPV 239
Cdd:MTH00183 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSgKKEP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00183 268 FGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00183 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00183 428 QHFLGLAG 435
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 544.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00077 30 GTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00077 108 SFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00077 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKeP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00077 268 FGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00077 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00077 428 QHFLGLAG 435
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 542.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00103 30 GTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00103 108 SFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00103 188 VLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKeP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00103 268 FGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00103 348 FTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00103 428 QHFLGLSG 435
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 541.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00007 27 GTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00007 105 ALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00007 185 VVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLeP 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00007 265 FGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00007 345 FTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFP 424
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00007 425 QHFLGLSG 432
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 531.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGnhLLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00079 31 GTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSiQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00079 109 SLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-V 239
Cdd:MTH00079 188 VFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKeV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFL 319
Cdd:MTH00079 268 FGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFL 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:MTH00079 348 FTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFP 427
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:MTH00079 428 LHFAGLHG 435
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
1-407 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 527.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:TIGR02891 24 GGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:TIGR02891 101 GGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:TIGR02891 181 ILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLF 320
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 321 TIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPM 400
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPM 420
|
....*..
gi 168418694 401 HFLGLAG 407
Cdd:TIGR02891 421 HLLGLLG 427
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-407 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 522.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:MTH00026 31 GTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:MTH00026 109 ALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFS-NKPV 239
Cdd:MTH00026 189 VFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSyKKQI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 240 FGYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEG--SIIFKTPMLFAIGFI 317
Cdd:MTH00026 269 FGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 318 FLFTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTF 397
Cdd:MTH00026 349 FLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITF 428
|
410
....*....|
gi 168418694 398 MPMHFLGLAG 407
Cdd:MTH00026 429 FPQHFLGLAG 438
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-407 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 518.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:COG0843 33 GGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:COG0843 110 GGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:COG0843 190 ALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLF 320
Cdd:COG0843 270 GYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILF 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 321 TIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPM 400
Cdd:COG0843 350 VIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPM 429
|
....*..
gi 168418694 401 HFLGLAG 407
Cdd:COG0843 430 HILGLLG 436
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
1-407 |
0e+00 |
|
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.
Pssm-ID: 238461 Cd Length: 463 Bit Score: 513.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNhlLLGNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPiMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd00919 19 GGLLALLIRLELATPGS--LFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:cd00919 96 GLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:cd00919 176 VLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLF 320
Cdd:cd00919 256 GYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 321 TIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPM 400
Cdd:cd00919 336 TIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPM 415
|
....*..
gi 168418694 401 HFLGLAG 407
Cdd:cd00919 416 HFLGLLG 422
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
1-407 |
3.24e-164 |
|
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238832 Cd Length: 501 Bit Score: 470.52 E-value: 3.24e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLLGNHqvYNVLITAHAFLMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:cd01662 25 GGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWS 160
Cdd:cd01662 102 GGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:cd01662 182 TLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLF 320
Cdd:cd01662 262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 321 TIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPM 400
Cdd:cd01662 342 VIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPM 421
|
....*..
gi 168418694 401 HFLGLAG 407
Cdd:cd01662 422 HILGLMG 428
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
4-407 |
1.43e-133 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 392.89 E-value: 1.43e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 4 MSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPVMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPPSLC 83
Cdd:MTH00048 34 LSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 84 LLLGSsmVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAgQTMYRIPLFVWSIFV 163
Cdd:MTH00048 112 FLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMT-NVFSRTSIILWSYLF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 164 TALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKP-VFGY 242
Cdd:MTH00048 189 TSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDdPFGY 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 243 IGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPML-FAIGFIFLFT 321
Cdd:MTH00048 269 YGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFT 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 322 IGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPMH 401
Cdd:MTH00048 349 IGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMH 428
|
....*.
gi 168418694 402 FLGLAG 407
Cdd:MTH00048 429 YFGLCG 434
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
1-407 |
1.13e-124 |
|
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.
Pssm-ID: 459678 Cd Length: 432 Bit Score: 367.28 E-value: 1.13e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 1 GGCMSMLIRMELAQPGNHLLlgNHQVYNVLITAHAFLMIFFMVMPvMIGGFGNWFVPIMIGSPDMAFPRLNNISFWLLPP 80
Cdd:pfam00115 17 GGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 81 SLCLLLGSSMvevGVGTGWTVYPPLssiqshsgASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMyRIPLFVWS 160
Cdd:pfam00115 94 GAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 161 IFVTALLLLLAVPVLAGAITMLLTDRNFNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVF 240
Cdd:pfam00115 162 ILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 241 GYIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIF-KTPMLFAIGFIFL 319
Cdd:pfam00115 236 GYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 320 FTIGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMP 399
Cdd:pfam00115 316 FIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFP 395
|
....*...
gi 168418694 400 MHFLGLAG 407
Cdd:pfam00115 396 MHILGLLG 403
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
6-407 |
6.04e-119 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 359.76 E-value: 6.04e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 6 MLIRMELAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVMIGGFgNWFVPIMIGSPDMAFPRLNNISFWLLPPSLCLL 85
Cdd:TIGR02843 78 MRTQQALASGGSAGYLPPHH-YDQIFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 86 lgssMVEVGVG----TGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWSI 161
Cdd:TIGR02843 156 ----NVSLGVGefaqTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 162 FVTALLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVFG 241
Cdd:TIGR02843 232 LCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRLFG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 242 YIGMVYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLFT 321
Cdd:TIGR02843 312 YTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 322 IGGLTGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPMH 401
Cdd:TIGR02843 392 IGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLY 471
|
....*.
gi 168418694 402 FLGLAG 407
Cdd:TIGR02843 472 ILGFMG 477
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
6-407 |
8.51e-102 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 316.11 E-value: 8.51e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 6 MLIRMELAQPGNHLLLGNHQvYNVLITAHAFLMIFFMVMPVMIGgFGNWFVPIMIGSPDMAFPRLNNISFWLLPPSLCLL 85
Cdd:PRK15017 79 MRSQQALASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILV 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 86 LGSSMVEVGVGTGWTVYPPLSSIQSHSGASVDLAIFSLHLSGASSILGAINFISTILNMRNAGQTMYRIPLFVWSIFVTA 165
Cdd:PRK15017 157 NVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCAN 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 166 LLLLLAVPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVFGYIGM 245
Cdd:PRK15017 237 VLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 246 VYAMISIGILGFIVWAHHMYTVGLDVDTRAYFTAATMIIAVPTGIKIFSWIATMWEGSIIFKTPMLFAIGFIFLFTIGGL 325
Cdd:PRK15017 317 VWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 326 TGIILANSGLDISLHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEVLGQIHFWSTFLGVNLTFMPMHFLGL 405
Cdd:PRK15017 397 TGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGF 476
|
..
gi 168418694 406 AG 407
Cdd:PRK15017 477 MG 478
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
200-407 |
3.04e-15 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 77.33 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 200 DPILYQHLFWFFGHPEVYILILPGFGIISHIVSTFSNKPVFGYIGMVYAMISIGILGFIVWAHHMYT-VGLDVDTRAYFT 278
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHM 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 168418694 279 AATMIIAVPTGIKIFSWIATM--------------WEGSIIFKTPMLFAIGF-IFLFTIGGLTGIILANSGLDISLHDTY 343
Cdd:cd01660 280 VLTFMVALPSLLTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTA 359
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 168418694 344 YVVAHFHYVLSMGAVFAIFAGFYYWFGKITGTQYPEV-LGQIHFWSTFLGVNLTFMPMHFLGLAG 407
Cdd:cd01660 360 WVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKrLALAQPWLWFVGMTIMSTAMHVAGLLG 424
|
|
| |
